Literature summary for 3.1.31.1 extracted from

Roche, J.; Caro, J.A.; Dellarole, M.; Guca, E.; Royer, C.A.; Garcia-Moreno, B.E.; Garcia, A.E.; Roumestand, C.
Structural, energetic, and dynamic responses of the native state ensemble of staphylococcal nuclease to cavity-creating mutations (2013), Proteins, 81, 1069-1080.

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Cloned(Commentary)

Cloned (Comment)	Organism
overexpression of wild-type and mutant enzymes in Escherichia coli	Staphylococcus aureus

Protein Variants

Protein Variants	Comment	Organism
F34A	site-directed mutagenesis	Staphylococcus aureus
I92A	site-directed mutagenesis, the mutant shows similar global stability like the wild-type enzyme	Staphylococcus aureus
L103A	site-directed mutagenesis, the mutant shows similar global stability like the wild-type enzyme	Staphylococcus aureus
L125A	site-directed mutagenesis, the mutant shows similar global stability like the wild-type enzyme	Staphylococcus aureus
L25A	site-directed mutagenesis	Staphylococcus aureus
L36A	site-directed mutagenesis	Staphylococcus aureus
L38A	site-directed mutagenesis	Staphylococcus aureus
additional information	ten cavity-containing variants of the highly stable form of the enzyme known as DELTA+PHS SNase are described, the DELTA+ PHS reference protein bears stabilizing substitutions in the C-terminal helix (G50F, V51N, P117G, H124L, and S128A), and a deletion of the mobile X loop (residues 44-49), which is part of the active site. Variants with substitutions in the C-terminal domain and the interface between alpha and beta subdomains showed large amide chemical shift variations relative to the parent protein, moderate, widespread, and compensatory perturbations of the H/D protection factors and increased local dynamics on a nanosecond time scale. In contrast, cavity creation in the beta-barrel subdomain leads to minimal perturbation of the structure of the folded state	Staphylococcus aureus
V23A	site-directed mutagenesis	Staphylococcus aureus
V66A	site-directed mutagenesis, the mutant shows similar global stability like the wild-type enzyme	Staphylococcus aureus
V74A	site-directed mutagenesis	Staphylococcus aureus

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant wild-type and mutant enzymes from Escherichia coli	Staphylococcus aureus

Synonyms

Synonyms	Comment	Organism
SNase	-	Staphylococcus aureus
staphylococcal nuclease	-	Staphylococcus aureus

General Information

General Information	Comment	Organism
additional information	the introduction of internal cavities into different subdomains affects local stability, flexibility, and dynamics of the enzyme, NMR spectroscopy under atmospheric and high pressure, H/D exchange and molecular dynamics simulations of wild-type and mutant enzymes, overview. Responses to the creation of cavities cannot be anticipated from global thermodynamic stability or crystal structures, they depend on the local structural and energetic context of the substitutions	Staphylococcus aureus

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Release 2023.1 (January 2023)